Catalysis by the isolated tryptophan tryptophylquinone-containing subunit of aromatic amine dehydrogenase is distinct from native enzyme and synthetic model compounds and allows further probing of TTQ mechanism

Biochemistry

Volumn 47, Issue 1, 2008, Pages 183-194

  Hothi, Parvinder ^a   Lee, Michael ^a   Cullis, Paul M ^b   Leys, David ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLAMINES; KINETIC ISOTOPE EFFECTS (KIE); TRYPTOPHYLQUINONE;

AMINES; AROMATIC COMPOUNDS; ISOTOPES; KINETICS; RATE CONSTANTS; SUBSTITUTION REACTIONS;

AMINO ACIDS;

AMINE DEHYDROGENASE; ARALKYLAMINE DEHYDROGENASE; BENZYLAMINE DERIVATIVE; OXIDOREDUCTASE; PHENETHYLAMINE; PHENYLHYDRAZINE; QUINONE DERIVATIVE; TRYPTOPHAN TRYPTOPHYLQUINONE; UNCLASSIFIED DRUG;

ARTICLE; BINDING KINETICS; CATALYSIS; CONFORMATIONAL TRANSITION; CORRELATION ANALYSIS; DEAMINATION; ENZYME ANALYSIS; ENZYME SUBUNIT; ENZYME SYNTHESIS; MOLECULAR MODEL; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINES; BENZYLAMINES; CATALYSIS; DIMERIZATION; INDOLEQUINONES; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PHENYLHYDRAZINES; PROTEIN SUBUNITS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

EID: 37849031515     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701690u     Document Type: Article

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